Denise C. Hocking, PhD, University of Rochester Medical Center

Denise C. Hocking, PhD
Denise C. Hocking, PhD

Native Human Fibronectin and Vitronectin contain multiple domains of interaction, such as those for sulfated glycosaminoglycans, gelatin, fibrin, and cell surface integrin receptors, and for integrins, urokinase receptors, plasminogen activator inhibitor, and glycosaminoglycans, respectively.

The Hocking lab focuses on understanding the mechanisms by which the extracellular matrix protein, fibronectin, affects cell and tissue functions that are critical for wound repair. Both structural mechanisms and intracellular signaling events that mediate cell and tissue responses to matrix fibronectin are studied. This information, in turn, is used to develop novel technologies for tissue engineering, and therapeutic approaches to promote tissue regeneration in chronic wounds.

These two dozen Human Fibronectin and Vitronectin Domain Variants isolate the various binding sites on the proteins for specific study.

The Investigator's Annexe Part of The Investigator's Annexe program.

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References

  1. Morla, A., Zhang, Z., and Ruoslahti, E. (1994) Superfibronectin is a functionally distinct form of fibronectin. Nature 367:193-196.
  2. Hocking, D.C., Sottile, J., and McKeown-Longo, P.J. (1994) Fibronectin's III 1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J. Biol. Chem 269:19183-19191.
  3. Hocking, D.C. and Kowalski, K. (2002) A cryptic fragment from fibronectin's III-1 module localizes to lipid rafts and stimulates cell growth and contractility. J. Cell Biol. 158: 175-184.
  4. Hocking, D.C., Smith, R.K., and McKeown-Longo, P.J. (1996) A novel role for the integrin-binding III10 module in fibronectin matrix assembly. J. Cell Biol. 133:431-444.
  5. Vakonakis, I., Staunton, D., Rooney, L.M., and Campbell, I. D. (2007) Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis. EMBO J. 26: 2575-2583.
  6. Roy, .C., Wilke-Mounts, S. and Hocking, D.C. (2011) Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate. Biomaterials 32(8): 2077-2087
  7. Wojciechowski, K., Chang, C.H., and Hocking, D.C. (2004) Expression, production, and characterization of full-length vitronectin inEscherichia coli. Protein Express. Purif. 36:131-138.
  8. Hocking, D.C., Sottile,J., Reho, T., Fassler, R., and McKeown-Lonngo, P.J. (1999) Inhibition of fibronectin matrix assembly by the heparin-binding domain of vitronectin. J. Biol. Chem. 274:27257-27273.
  9. Wilkins-Port, C.E., Sanderson, R.D., Tominna-Sebald, E.T., and McKeown-Longo, P.J. (2003) Vitronectin's basic domain is a syndecan ligand which functions in trans to regulate vitronectin turnover. Cell Commun. Adhes. 10: 85-103